Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

7. Enzyme Inhibition and Regulation

Apparent Km and Vmax

Biochemistry

7. Enzyme Inhibition and Regulation

Apparent Km and Vmax

Previous problemNext problem

Struggling with Biochemistry?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

Uncompetitive inhibitor A at a concentration of 4 mM cuts the K _m^app in half for an enzymatic reaction, whereas the K_m^app is one-fourth the K_m in the presence of 18 mM uncompetitive inhibitor B. What is the ratio of the K'_I for inhibitor A to the K'_I for inhibitor B?

3/2

2/3

1/3

Previous problemNext problem

Verified step by step guidance

Understand that uncompetitive inhibition affects both the apparent Michaelis constant (K'm) and the maximum velocity (V'max) of an enzyme-catalyzed reaction. The relationship is given by: K'm = Km / (1 + [I]/K'I), where [I] is the inhibitor concentration and K'I is the inhibition constant.

For inhibitor A, we know that K'm is half of Km at 4 mM concentration. Set up the equation: Km / 2 = Km / (1 + 4/K'I_A). Simplify to find the relationship: 1 + 4/K'I_A = 2.

Solve the equation for K'I_A: 4/K'I_A = 1, which implies K'I_A = 4 mM.

For inhibitor B, K'm is one-fourth of Km at 18 mM concentration. Set up the equation: Km / 4 = Km / (1 + 18/K'I_B). Simplify to find the relationship: 1 + 18/K'I_B = 4.

Solve the equation for K'I_B: 18/K'I_B = 3, which implies K'I_B = 6 mM. Finally, calculate the ratio of K'I_A to K'I_B: K'I_A / K'I_B = 4/6 = 2/3.